CCD57_MOUSE
ID CCD57_MOUSE Reviewed; 1016 AA.
AC Q6PHN1;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Coiled-coil domain-containing protein 57 {ECO:0000305};
GN Name=Ccdc57 {ECO:0000312|MGI:MGI:1918526};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP FUNCTION.
RX PubMed=32402286; DOI=10.1016/j.celrep.2020.107630;
RA Gurkaslar H.K., Culfa E., Arslanhan M.D., Lince-Faria M.,
RA Firat-Karalar E.N.;
RT "CCDC57 Cooperates with Microtubules and Microcephaly Protein CEP63 and
RT Regulates Centriole Duplication and Mitotic Progression.";
RL Cell Rep. 31:107630-107630(2020).
CC -!- FUNCTION: Pleiotropic regulator of centriole duplication, mitosis, and
CC ciliogenesis (PubMed:32402286). Critical interface between centrosome
CC and microtubule-mediated cellular processes. Centriole duplication
CC protein required for recruitment of CEP63, CEP152, and PLK4 to the
CC centrosome. Independent of its centrosomal targeting, localizes to and
CC interacts with microtubules and regulates microtubule nucleation,
CC stability, and mitotic progression (By similarity).
CC {ECO:0000250|UniProtKB:Q2TAC2, ECO:0000269|PubMed:32402286}.
CC -!- SUBUNIT: Interacts with CEP63; the interaction is required for their
CC location to proximal end of centrioles. Interacts with microtubules.
CC {ECO:0000250|UniProtKB:Q2TAC2}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250|UniProtKB:Q2TAC2}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome, centriolar
CC satellite {ECO:0000250|UniProtKB:Q2TAC2}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome, centriole
CC {ECO:0000250|UniProtKB:Q2TAC2}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250|UniProtKB:Q2TAC2}. Note=Localizes to resolvable rings at
CC the proximal end of centrioles. In mitotic cells, localizes to spindle
CC microtubules during metaphase. {ECO:0000250|UniProtKB:Q2TAC2}.
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DR EMBL; AL662901; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL663090; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC056480; AAH56480.1; -; mRNA.
DR CCDS; CCDS25760.1; -.
DR RefSeq; NP_082021.1; NM_027745.1.
DR RefSeq; XP_017170256.1; XM_017314767.1.
DR AlphaFoldDB; Q6PHN1; -.
DR SMR; Q6PHN1; -.
DR STRING; 10090.ENSMUSP00000050996; -.
DR iPTMnet; Q6PHN1; -.
DR PhosphoSitePlus; Q6PHN1; -.
DR EPD; Q6PHN1; -.
DR MaxQB; Q6PHN1; -.
DR PaxDb; Q6PHN1; -.
DR PRIDE; Q6PHN1; -.
DR ProteomicsDB; 265711; -.
DR Antibodypedia; 19887; 60 antibodies from 11 providers.
DR Ensembl; ENSMUST00000056781; ENSMUSP00000050996; ENSMUSG00000048445.
DR GeneID; 71276; -.
DR KEGG; mmu:71276; -.
DR UCSC; uc007muv.1; mouse.
DR CTD; 284001; -.
DR MGI; MGI:1918526; Ccdc57.
DR VEuPathDB; HostDB:ENSMUSG00000048445; -.
DR eggNOG; ENOG502QSW3; Eukaryota.
DR GeneTree; ENSGT00940000153251; -.
DR HOGENOM; CLU_011424_1_0_1; -.
DR InParanoid; Q6PHN1; -.
DR OMA; WKFDDEL; -.
DR OrthoDB; 490834at2759; -.
DR PhylomeDB; Q6PHN1; -.
DR TreeFam; TF333001; -.
DR BioGRID-ORCS; 71276; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Ccdc57; mouse.
DR PRO; PR:Q6PHN1; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q6PHN1; protein.
DR Bgee; ENSMUSG00000048445; Expressed in seminiferous tubule of testis and 75 other tissues.
DR Genevisible; Q6PHN1; MM.
DR GO; GO:0034451; C:centriolar satellite; ISS:UniProtKB.
DR GO; GO:0005814; C:centriole; ISS:UniProtKB.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005876; C:spindle microtubule; ISS:UniProtKB.
DR GO; GO:0007099; P:centriole replication; ISS:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0007020; P:microtubule nucleation; ISS:UniProtKB.
DR GO; GO:0045931; P:positive regulation of mitotic cell cycle; ISS:UniProtKB.
DR InterPro; IPR042481; CCDC57.
DR PANTHER; PTHR46725; PTHR46725; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Cytoskeleton; Reference proteome.
FT CHAIN 1..1016
FT /note="Coiled-coil domain-containing protein 57"
FT /id="PRO_0000288872"
FT REGION 1..503
FT /note="Centrosomal targeting domain"
FT /evidence="ECO:0000250|UniProtKB:Q2TAC2"
FT REGION 500..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 549..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 604..1016
FT /note="Microtubule binding domain"
FT /evidence="ECO:0000250|UniProtKB:Q2TAC2"
FT REGION 781..921
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 933..1016
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 14..607
FT /evidence="ECO:0000255"
FT COILED 676..700
FT /evidence="ECO:0000255"
FT COILED 748..775
FT /evidence="ECO:0000255"
FT COMPBIAS 844..858
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 896..914
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 935..949
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 995..1009
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1016 AA; 116194 MW; F62A2086A7B155D0 CRC64;
MLPLCSEREL NELLARKEEE WRVLQAHRAQ LQEAALQAAQ NRLEETQGKL QRLQEDFVYN
LQVLEERDRE LERYDVEFTQ ARQREEAQQA EASELKIEVA KLKQDLTREA RRVGELQHQH
QLMLQEHRLE LERVHSDKNS ELAHQREQNE RLEWELERKL KELDGELALQ RQELLLEFES
KMQRREHEFQ LRADDMSNVV LTHELKIKLL NKELQALRDA GARAAESLQK AEAEHVELER
KLQERARELQ DLEAVKDARI KGLEKKLYSA QLAKKKAEET FRRKHEELDR QAREKDTVLA
AVKRAHAEEL QTLDAKVLEL QFLCETLEGQ LRRAECTRAE DAKEKNALTD KFREDAAALK
AAWDAQITQM SKETVSKDFQ IHTLQEEEMK LKAQVARFQQ DIDRYKQQLS LAVERGQSLE
REQVQLGLDW QRRCDDIERD QIQKSETLIE GLTKARDQVA AKLQETEKAL RQQETLLKAV
SLERDQAMET LRTHGLLPGQ EAQVPPQQHE GEIRADSPST EIQRLQEQNA GLRNAVSQMR
REMEMLSGHL PPAQPEECSN ADPDPKAGGD STPPDYVLTL EAEMQNLKHK LKALEEQLQS
TEEPVKTSVA TADPHHGVHS SAAAADAALA DQTSTALALR KLGDRVHLLN LLVTQLKRKL
RQKPRELVPV QHEVPSEVDQ VHLEVLELQK QVAELRKHLK VTPQGEPSSR EQLQRQGVAD
RYPMGMEDQT ESPTFPQEGA QPPQTIYVTH LQRKLKDAAR KILSLRLERE QLLEMGNRLR
AEQGHAKGKP TPCPGPPTSE PQDPQEVPER SLDRGPPLGQ LQPYSTTQDP RHTKRRCASE
YAGKSQPHSA QVGSKTNTPR GHKAEMASRP AQLSQKQHRI PTETWKPVYQ KENRTPKLPQ
AHEVPEESDH RTHRSSSLAS SSLQDIWRLL ELGSSPSGVP SQDNSVAECP APSRPSCFQK
VNRSPVPIQK AFAVKGLKME AQPKATPPRP SKSHPAKPTN CQQQRPSRIR NYNLKD
